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Asthenozoospermia is considered as a common cause of male infertility and characterized by reduced sperm motility. However, the molecular mechanism that impairs sperm motility remains unknown in most cases. In the present review, we briefly reviewed the proteome of spermatozoa and seminal plasma in asthenozoospermia and considered post-translational modifications in spermatozoa of asthenozoospermia. The reduction of sperm motility in asthenozoospermic patients had been attributed to factors, for instance, energy metabolism dysfunction or structural defects in the sperm-tail protein components and the differential proteins potentially involved in sperm motility such as COX6B, ODF, TUBB2B were described. Comparative proteomic analysis open a window to discover the potential pathogenic mechanisms of asthenozoospermia and the biomarkers with clinical significance.

Unlabelled: Lysine acetylation, a ubiquitous and conserved posttranslational modification, has recently been shown to participate in many diverse non-chromatin-associated biological processes in prokaryotes and eukaryotes. However, the full extent and functional significance of acetylation in Schistosoma japonicum is still unknown. To investigate the nature, extent, and biological functions of lysine acetylation in schistosomes, immunoaffinity-based acetyl-lysine peptide enrichment, integrated with mass spectrometry, was used to comprehensively characterize the lysine-acetylated proteins in this parasite. In total, 1109 acetylated proteins and 2393 acetylation sites in S. japonicum were identified, representing the largest acetylome yet reported in a parasite. In a bioinformatic analysis showed that these acetylated proteins were mainly enriched in the biological process categories of metabolism, gene expression, translation, and transport. The classification according to molecular function revealed that the largest class involved the catalytic activity of different enzymes, including oxidoreductase, transferase, and pyrophosphatase activities. Most of the acetylated proteins in the cellular component category occurred in the cytoplasm, membrane, cytoskeleton, and nucleus. These data demonstrate the generality of lysine acetylation and provide the first global survey of acetylation in schistosomes. Our findings are an exciting starting point for the further exploration of the functions of acetylation in the biology of this parasite., Significance: Schistosomiasis is one of the world's most prevalent and neglected tropical parasitic zoonotic diseases, and it causes almost 200,000 deaths annually. To control and eradicate schistosomiasis, effective vaccines are urgently required, and drug targets that are essential for schistosome survival must be identified in fundamental studies of schistosome biology. Posttranslational modifications are complex, fundamental, and important mechanisms that regulate the physiological functions of organisms. Lysine acetylation, a ubiquitous and conserved posttranslational modification, has recently been shown to participate in many diverse non-chromatin-associated biological processes in prokaryotes and eukaryotes. However, the full extent and functional significance of acetylation in Schistosoma japonicum is still unknown. To investigate the nature, extent, and biological functions of lysine acetylation in S. japonicum, we employ immunoaffinity-based acetyl-lysine peptide enrichment, integrated with mass spectrometry to comprehensively characterize the lysine-acetylated proteins in this parasite. The results of our data demonstrate the generality of lysine acetylation and provide the first global survey of acetylation in schistosomes. Our findings are an exciting starting point for the further exploration of the functions of acetylation in the biology of this parasite. Meanwhile, identifying the mechanisms and proteins targeted by acetylation may also provide a promising avenue for specific drug design and the development of sophisticated therapeutic strategies., (Copyright © 2016 Elsevier B.V. All rights reserved.)

Schistosomiasis remains a serious public health problem with 200 million people infected and 779 million people at risk worldwide. The schistosomulum and adult worm are two stages of the complex lifecycle of Schistosoma japonicum and excretory/secretory proteins (ESPs) play a major role in host-parasite interactions. In this study, iTRAQ-coupled LC-MS/MS was used to investigate the proteome of ESPs obtained from schistosomula and adult worms of S. japonicum, and 298 differential ESPs were identified. Bioinformatics analysis of differential ESPs in the two developmental stages showed that 161 ESPs upregulated in schistosomula were associated with stress responses, carbohydrate metabolism and protein degradation, whereas ESPs upregulated in adult worms were mainly related to immunoregulation and purine metabolism. Recombinant heat shock protein 70 (HSP70) and thioredoxin peroxidase (TPx), two differential proteins identified in this study, were expressed. Further studies showed that rSjHSP70 and rSjTPx stimulated macrophages expressing high levels of the anti-inflammatory factors TGF-β, IL-10 and Arg-1, and suppressed the expression of the pro-inflammatory cytokines TNF-α, IL-1β, IL-6 and iNOS in LPS-induced macrophages. This study provides new insights into the survival and development of schistosomes in the final host and helps identify vaccine candidates or new diagnostic reagents for schistosomiasis., (Copyright © 2016 Elsevier B.V. All rights reserved.)

Schistosomiasis remains a serious public health problem, with 200 million people infected and 779 million people at risk worldwide. The schistosomulum is the early stage of the complex lifecycle of Schistosoma japonicum in their vertebrate hosts, and is the main target of vaccine-induced protective immunity. Excretory/secretory (ES) proteins play a major role in host-parasite interactions and ES protein compositions of schistosomula of S. japonicum have not been characterized to date. In the present study, the proteome of ES proteins from 14 day schistosomula of S. japonicum was analyzed by liquid chromatography/tandem mass spectrometry and 713 unique proteins were finally identified. Gene ontology and pathway analysis revealed that identified proteins were mainly involved in carbohydrate metabolism, degradation, response to stimulus, oxidation-reduction, biological regulation and binding. Flow cytometry analysis demonstrated that thioredoxin peroxidase identified in this study had the effect on inhibiting MHCII and CD86 expression on LPS-activated macrophages. The present study provides insight into the growth and development of the schistosome in the final host and valuable information for screening vaccine candidates for schistosomiasis., (Copyright © 2015 Elsevier B.V. All rights reserved.)

The aim of this study was to search for immunogenic schistosomula proteins in the hope of identifying novel intervention targets. Schistosomula proteins were analyzed by immunoproteomic which the probes were sera derived from BALB/c mice (susceptible hosts) and Microtus fortis (resistant hosts). A total of 116 immunoreactive proteins recognized by 10 days post-infected BALB/c mice, M. fortis sera, and uninfected M. fortis sera were selected for further analysis. Finally, 95 protein spots were identified by mass spectrometry (MS) analysis. Bioinformatics analysis showed that the differentially identified immunogenic proteins participated mainly in cytoskeleton organization, cell motility, energy metabolism, responses to stimuli, and protein folding. Many of these proteins were the tegument or excretory-secretory products of schistosomes reported in previous studies. Among of them, Schistosoma japonicum DnaJ (Hsp40) homologue (SjDnaJ) was successfully expressed and the purified recombinant product was evaluated by immunoprotective experiment. After immunization of BALB/c mice with recombinant SjDnaJ, it could induce 34.5% and 48.9% reductions in the numbers of worms and eggs in the liver. These results contribute to a better understanding of the molecular mechanisms underlying the host-parasite relationship and provide a major dataset to facilitate the further development of new vaccine candidates and/or diagnostic markers for schistosomiasis., Biological Significance: Schistosomiasis is caused by parasitic blood-dwelling flukes in tropical and subtropical areas, and it is one of the world's most prevalent tropical diseases. The lack of effective vaccine and reliable diagnostic methods make this disease difficult to control. In China, S. japonicum can infect more than 40 different susceptible mammals for this parasite. However, M. fortis is the only known mammal where the schistosome cannot develop and it exhibits no significant pathological effects. Many studies' results showed that native antibodies against S. japonicum are present in M. fortis that may have important anti-schistosomiasis roles during the infection process. The aim of this study was to search for immunogenic schistosomula proteins in the hope of identifying novel intervention targets. We present a comparative immunoproteomics analysis of the proteins recognized by susceptible and resistant host antibodies before and 10-days after infections. The results of this analysis will be helpful for identifying the key molecules required for the survival and development of schistosomes. At the same time, the study contributes to a better understanding of the molecular mechanisms underlying the host-parasite relationship associated with schistosomes and they also provide a major dataset to facilitate the further development of new diagnostic assays and/or vaccine candidates for schistosomiasis., (Copyright © 2015 Elsevier B.V. All rights reserved.)